scholarly journals Role of the highly conserved G68 residue in the yeast phosphorelay protein Ypd1: implications for interactions between histidine phosphotransfer (HPt) and response regulator proteins

2019 ◽  
Vol 20 (1) ◽  
Author(s):  
Emily N. Kennedy ◽  
Skyler D. Hebdon ◽  
Smita K. Menon ◽  
Clay A. Foster ◽  
Daniel M. Copeland ◽  
...  
Keyword(s):  
Response Regulator ◽  
Histidine Phosphotransfer

scholarly journals Role of the RprY response regulator in P. gingivalis community development and virulence

2020 ◽  
Vol 35 (6) ◽  
pp. 231-239
Author(s):  
Daonan Shen ◽  
John D. Perpich ◽  
Kendall S. Stocke ◽  
Lan Yakoumatos ◽  
Zackary R. Fitzsimonds ◽  
...  
Keyword(s):  
Community Development ◽  
Response Regulator

Transcriptional regulation of a hybrid cluster (prismane) protein

2005 ◽  
Vol 33 (1) ◽  
pp. 195-197 ◽  
Author(s):  
N.A. Filenko ◽  
D.F. Browning ◽  
J.A. Cole
Keyword(s):  
Physiological Function ◽  
Response Regulator ◽  
Anaerobic Growth ◽  
Hybrid Cluster ◽  
E Coli ◽  
Mutant Strains ◽  
Translation Initiation Codon ◽  
Nitric Oxide Reduction ◽  
Nitrate And Nitrite

HCP (hybrid-cluster protein) contains two Fe/S clusters, one of which is a hybrid [4Fe-2S-2O] cluster. Despite intensive study, its physiological function has not been reported. The Escherichia coli hcp gene is located in a two-gene operon with hcr, which encodes an NADH-dependent HCP reductase. E. coli HCP is detected after anaerobic growth with nitrate or nitrite: possible roles for it in hydroxylamine or nitric oxide reduction have been proposed. To study the regulation and role of HCP, an hcp::lacZ fusion was constructed and transformed into fnr, arcA and norR mutant strains of E. coli. Transcription from the hcp promoter was induced during anaerobic growth. Only the fnr mutant was defective in hcp expression. Nitrate- and nitrite-induced transcription from the hcp promoter was activated by the response regulator proteins NarL and NarP. Gel retardation assays were used to show that FNR (fumarate-nitrate regulation) and NarL form a complex with the hcp promoter. Transcription of the hcp-hcr operon initiates at a thymine nucleotide located 31 bp upstream of the translation-initiation codon. HCP has been overexpressed from a recombinant plasmid for physiological studies.

scholarly journals Crystal Structure of the CheA Histidine Phosphotransfer Domain that Mediates Response Regulator Phosphorylation in Bacterial Chemotaxis

2001 ◽  
Vol 276 (33) ◽  
pp. 31074-31082 ◽  
Author(s):  
Lionel Mourey ◽  
Sandra Da Re ◽  
Jean-Denis Pédelacq ◽  
Tatiana Tolstykh ◽  
Cécile Faurie ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Response Regulator ◽  
Bacterial Chemotaxis ◽  
Histidine Phosphotransfer

scholarly journals A universal stress protein in Mycobacterium smegmatis sequesters the cAMP-regulated lysine acyltransferase and is essential for biofilm formation

2019 ◽  
Vol 295 (6) ◽  
pp. 1500-1516 ◽  
Author(s):  
Sintu Samanta ◽  
Priyanka Biswas ◽  
Arka Banerjee ◽  
Avipsa Bose ◽  
Nida Siddiqui ◽  
...  
Keyword(s):  
Stress Responses ◽  
Mycobacterium Smegmatis ◽  
Biofilm Formation ◽  
Stress Proteins ◽  
Response Regulator ◽  
Stress Protein ◽  
Colony Morphology ◽  
Regulator Gene ◽  
Its Gene

Universal stress proteins (USPs) are present in many bacteria, and their expression is enhanced under various environmental stresses. We have previously identified a USP in Mycobacterium smegmatis that is a product of the msmeg_4207 gene and is a substrate for a cAMP-regulated protein lysine acyltransferase (KATms; MSMEG_5458). Here, we explored the role of this USP (USP4207) in M. smegmatis and found that its gene is present in an operon that also contains genes predicted to encode a putative tripartite tricarboxylate transporter (TTT). Transcription of the TTT-usp4207 operon was induced in the presence of citrate and tartrate, perhaps by the activity of a divergent histidine kinase-response regulator gene pair. A usp4207-deleted strain had rough colony morphology and reduced biofilm formation compared with the WT strain; however, both normal colony morphology and biofilm formation were restored in a Δusp4207Δkatms strain. We identified several proteins whose acetylation was lost in the Δkatms strain, and whose transcript levels increased in M. smegmatis biofilms along with that of USP4207, suggesting that USP4207 insulates KATms from its other substrates in the cell. We propose that USP4207 sequesters KATms from diverse substrates whose activities are down-regulated by acylation but are required for biofilm formation, thus providing a defined role for this USP in mycobacterial physiology and stress responses.

scholarly journals The role of Acinetobacter baumannii response regulator BfmR in pellicle formation and competitiveness via contact-dependent inhibition system

2019 ◽  
Vol 19 (1) ◽  
Author(s):  
Renatas Krasauskas ◽  
Jūratė Skerniškytė ◽  
Julija Armalytė ◽  
Edita Sužiedėlienė
Keyword(s):  
Acinetobacter Baumannii ◽  
Transcriptional Activation ◽  
Related Species ◽  
Response Regulator ◽  
Multi Drug Resistance ◽  
Clinical Environment ◽  
Acinetobacter Baylyi ◽  
Pellicle Formation ◽  
Dependent Inhibition

Abstract Background Acinetobacter baumannii is one of the most important opportunistic pathogens responsible for hospital acquired infections. It displays multi-drug resistance profile and has the ability to colonize surfaces and persist under harsh conditions. A. baumannii two-component signal transduction system BfmRS, consisting of response regulator BfmR and sensor kinase BfmS, has been implicated in the control of various virulence-related traits and has been suggested to act as a global modulator of A. baumannii physiology. Results Here, we assessed the role of BfmR regulator in pellicle formation and bacterial competition, features important for the establishment of A. baumannii in clinical environment. We show that BfmR is required for the pellicle formation of A. baumannii, as ΔbfmRS mutant lacked this phenotype. The loss of bfmRS also greatly reduced the secretion of A. baumannii Hcp protein, which is a component of T6SS secretion system. However, T6SS-mediated killing phenotype was not impaired in ΔbfmRS mutant. On the contrary, the same mutation resulted in the transcriptional activation of contact-dependent inhibition (CDI) system, which A. baumannii used to inhibit the growth of another clinical A. baumannii strain and a closely related species Acinetobacter baylyi. Conclusions The obtained results indicate that BfmR is not only required for the pellicle phenotype induction in A. baumannii, but also, due to the down-regulation of a CDI system, could allow the incorporation of other A. baumannii strains or related species, possibly increasing the likelihood of the pathogens’ survival.

scholarly journals Identification of a Streptococcus pneumoniae Gene Locus Encoding Proteins of an ABC Phosphate Transporter and a Two-Component Regulatory System

1999 ◽  
Vol 181 (4) ◽  
pp. 1126-1133 ◽  
Author(s):  
Rodger Novak ◽  
Anje Cauwels ◽  
Emmanuelle Charpentier ◽  
Elaine Tuomanen
Keyword(s):  
Response Regulator ◽  
Regulatory System ◽  
Phosphate Limitation ◽  
Pho Regulon ◽  
Loss Of Function ◽  
Gene Encoding ◽  
E Coli ◽  
Two Component ◽  
Pst System

ABSTRACT The Escherichia coli Pst system belongs to the family of ABC transporters. It is part of a phosphate (PHO) regulon which is regulated by extracellular phosphate. Under conditions of phosphate limitation, the response regulator PhoB is phosphorylated by the histidine kinase PhoR and binds to promoters that share a consensus PHO box. Under conditions of phosphate excess, PhoR, Pst, and PhoU downregulate the PHO regulon. Screening of a library of pneumococcal mutants with defects in exported proteins revealed a putative two-component regulatory system, PnpR-PnpS, and a downstream ABC transporter, similar to the Pst system in E. coli including a gene encoding a PhoU protein. Similar to E. coli, mutagenesis of the ATP-binding cassette gene, pstB, resulted in decreased uptake of phosphate. The effects of the loss of the pneumococcal Pst system extended to decreased transformation and lysis. Withdrawal of phosphate led to transformation deficiency in the parent strain R6x but not to penicillin tolerance, suggesting that reduced bacterial death was independent of phosphate. None of these phenotypes was observed in the pneumococcal loss-of-function mutantphoU. By using a lacZ reporter construct, it was demonstrated that expression of the two-component regulatory system PnpR-PnpS was not influenced by different concentrations of phosphate. These results suggest a more complex role of the Pst system in pneumococcal physiology than in that of E. coli.

scholarly journals Insight into the essential role of the Helicobacter pylori HP1043 orphan response regulator: genome-wide identification and characterization of the DNA-binding sites

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Simone Pelliciari ◽  
Eva Pinatel ◽  
Andrea Vannini ◽  
Clelia Peano ◽  
Simone Puccio ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Binding Sites ◽  
Essential Role ◽  
Response Regulator ◽  
Dna Binding Sites ◽  
Genome Wide ◽  
Identification And Characterization ◽  
Insight Into

scholarly journals Colonization and Inflammation Deficiencies in Mongolian Gerbils Infected by Helicobacter pylori Chemotaxis Mutants

2005 ◽  
Vol 73 (3) ◽  
pp. 1820-1827 ◽  
Author(s):  
David J. McGee ◽  
Melanie L. Langford ◽  
Emily L. Watson ◽  
J. Elliot Carter ◽  
Yu-Ting Chen ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Immune Cell ◽  
Response Regulator ◽  
Critical Role ◽  
Mongolian Gerbils ◽  
Wild Type ◽  
In The Wild ◽  
H Pylori

ABSTRACT Helicobacter pylori causes disease in the human stomach and in mouse and gerbil stomach models. Previous results have shown that motility is critical for H. pylori to colonize mice, gerbils, and other animal models. The role of chemotaxis, however, in colonization and disease is less well understood. Two genes in the H. pylori chemotaxis pathway, cheY and tlpB, which encode the chemotaxis response regulator and a methyl-accepting chemoreceptor, respectively, were disrupted. The cheY mutation was complemented with a wild-type copy of cheY inserted into the chromosomal rdxA gene. The cheY mutant lost chemotaxis but retained motility, while all other strains were motile and chemotactic in vitro. These strains were inoculated into gerbils either alone or in combination with the wild-type strain, and colonization and inflammation were assessed. While the cheY mutant completely failed to colonize gerbil stomachs, the tlpB mutant colonized at levels similar to those of the wild type. With the tlpB mutant, there was a substantial decrease in inflammation in the gerbil stomach compared to that with the wild type. Furthermore, there were differences in the numbers of each immune cell in the tlpB-mutant-infected stomach: the ratio of lymphocytes to neutrophils was about 8 to 1 in the wild type but only about 1 to 1 in the mutant. These results suggest that the TlpB chemoreceptor plays an important role in the inflammatory response while the CheY chemotaxis regulator plays a critical role in initial colonization. Chemotaxis mutants may provide new insights into the steps involved in H. pylori pathogenesis.

scholarly journals Role of two-component sensory systems of Salmonella enterica serovar Dublin in the pathogenesis of systemic salmonellosis in cattle

Microbiology ◽  
2010 ◽  
Vol 156 (10) ◽  
pp. 3108-3122 ◽  
Author(s):  
Gillian D. Pullinger ◽  
Pauline M. van Diemen ◽  
Francis Dziva ◽  
Mark P. Stevens
Keyword(s):  
Salmonella Enterica ◽  
Response Regulator ◽  
Systemic Disease ◽  
Lymphatic Vessels ◽  
Intestinal Barrier ◽  
Systemic Infection ◽  
Oral Route ◽  
Systematic Analysis ◽  
Two Component

Salmonella enterica serovar Dublin (S. Dublin) is associated with enteritis, typhoid and abortion in cattle. Infections are acquired by the oral route, and the bacteria transit through varied anatomical and cellular niches to elicit systemic disease. S. Dublin must therefore sense and respond to diverse extrinsic stimuli to control gene expression in a spatial and temporal manner. Two-component systems (TCSs) play key roles in such processes, and typically contain a membrane-associated sensor kinase (SK) that modifies a cognate response regulator. Analysis of the genome sequence of S. Dublin identified 31 conserved SK genes. Each SK gene was separately disrupted by lambda Red recombinase-mediated insertion of transposons harbouring unique sequence tags. Calves were challenged with a pool of the mutants together with control strains of defined virulence by the oral and intravenous routes. Quantification of tagged mutants in output pools derived from various tissues and cannulated lymphatic vessels allowed the assignment of spatial roles for each SK following oral inoculation or when the intestinal barrier was bypassed by intravenous delivery. Mutant phenotypes were also assigned in cultured intestinal epithelial cells. Mutants with insertions in barA, envZ, phoQ, ssrA or qseC were significantly negatively selected at all enteric and systemic sites sampled after oral dosing. Mutants lacking baeS, dpiB or citA were negatively selected at some but not all sites. After intravenous inoculation, only barA and phoQ mutants were significantly under-represented at systemic sites. The novel role of baeS in intestinal colonization was confirmed by oral co-infection studies, with a mutant exhibiting modest but significant attenuation at a number of enteric sites. This is the first systematic analysis of the role of all Salmonella TCSs in a highly relevant model of enteric fever. Spatial roles were assigned to eight S. Dublin SKs, but most were not essential for intestinal or systemic infection of the target host.

Evidence against the physiological role of acetyl phosphate in the phosphorylation of the ArcA response regulator in Escherichia coli

2009 ◽  
Vol 47 (5) ◽  
pp. 657-662 ◽  
Author(s):  
Xueqiao Liu ◽  
Gabriela R. Peña Sandoval ◽  
Barry L. Wanner ◽  
Won Seok Jung ◽  
Dimitris Georgellis ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Response Regulator ◽  
Physiological Role ◽  
Acetyl Phosphate
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